Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q39K91

- HISX_BURS3

UniProt

Q39K91 - HISX_BURS3

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei138 – 1381NADUniRule annotation
Binding sitei199 – 1991NADUniRule annotation
Binding sitei222 – 2221NADUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Metal bindingi270 – 2701ZincUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Active sitei335 – 3351Proton acceptorUniRule annotation
Active sitei336 – 3361Proton acceptorUniRule annotation
Binding sitei336 – 3361SubstrateUniRule annotation
Metal bindingi369 – 3691ZincUniRule annotation
Binding sitei369 – 3691SubstrateUniRule annotation
Binding sitei423 – 4231SubstrateUniRule annotation
Metal bindingi428 – 4281ZincUniRule annotation
Binding sitei428 – 4281SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciBSP269483:GHLS-357-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:Bcep18194_A3523
OrganismiBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
Taxonomic identifieri482957 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000002705: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Histidinol dehydrogenasePRO_0000229853Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi269483.Bcep18194_A3523.

Structurei

3D structure databases

ProteinModelPortaliQ39K91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39K91-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSITIRKLDS TSAGFGAELR ALLAFEASED AAIEQSVAQI LADVKSRGDA
60 70 80 90 100
AVLEYTNRFD RLSASSIAAL ELPQDALQTA LDSLAPKARA ALEAAAARVR
110 120 130 140 150
AYHEKQKIEC GTHSWQYTES DGTVLGQKVT PLDRVGLYVP GGKAAYPSSV
160 170 180 190 200
LMNAIPARVA GVGEIVMVVP TPDGVKNDLV LAAALLGGVD RVFTIGGAQA
210 220 230 240 250
VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM IAGPSEILVL
260 270 280 290 300
CDGTTDPNWV AMDLFSQAEH DELAQSILLC PDGAFLERVE KAIDELLPSM
310 320 330 340 350
PRQDVIRASL EGRGALIKVR DMAEACRIAN DIAPEHLEIS ALEPQQWGQQ
360 370 380 390 400
IRHAGAIFLG RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS
410 420 430
LIEVSAEGAQ TLGEIASELA YGEGLQAHAK SAEFRMKH
Length:438
Mass (Da):46,414
Last modified:November 22, 2005 - v1
Checksum:i2CD2FBB3520628C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000151 Genomic DNA. Translation: ABB07125.1.
RefSeqiWP_011350726.1. NC_007510.1.
YP_367769.1. NC_007510.1.

Genome annotation databases

EnsemblBacteriaiABB07125; ABB07125; Bcep18194_A3523.
GeneIDi3748700.
KEGGibur:Bcep18194_A3523.
PATRICi19284314. VBIBurSp120713_1598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000151 Genomic DNA. Translation: ABB07125.1 .
RefSeqi WP_011350726.1. NC_007510.1.
YP_367769.1. NC_007510.1.

3D structure databases

ProteinModelPortali Q39K91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269483.Bcep18194_A3523.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB07125 ; ABB07125 ; Bcep18194_A3523 .
GeneIDi 3748700.
KEGGi bur:Bcep18194_A3523.
PATRICi 19284314. VBIBurSp120713_1598.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci BSP269483:GHLS-357-MONOMER.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome 1 of Burkholderia sp. 383."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 383.

Entry informationi

Entry nameiHISX_BURS3
AccessioniPrimary (citable) accession number: Q39K91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: October 1, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3